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Immobilization Increases the Stability and Reusability of Pigeon Pea NADP+ Linked Glucose-6-Phosphate Dehydrogenase

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Abstract

Immobilization of enzymes is valuably important as it improves the stability and hence increases the reusability of enzymes. The present investigation is an attempt for immobilization of purified glucose-6-phosphate dehydrogenase from pigeon pea on different matrix. Maximum immobilization was achieved when alginate was used as immobilization matrix. As compared to soluble enzyme the alginate immobilized enzyme exhibited enhanced optimum pH and temperature. The alginate immobilized enzyme displayed more than 80% activity up to 7 continuous reactions and more than 50% activity up to 11 continuous reactions.

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Abbreviations

G6PD:

Glucose-6-phosphate dehydrogenase

NADP+ :

Nicotinamide adenine dinucleotide phosphate (oxidized)

NADPH:

Nicotinamide adenine dinucleotide phosphate (reduced)

ATP:

Adenosine triphosphate

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Acknowledgements

Author is highly grateful to Department of Biotechnology, Government of India for providing research grant BT/04/NE/2009 under the project “Institutional Biotechnology Hub” at College of Horticulture & Forestry, Central Agricultural University, Pasighat-791102, Arunachal Pradesh.

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Correspondence to Siddhartha Singh.

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Singh, S., Singh, A.K., Singh, M.C. et al. Immobilization Increases the Stability and Reusability of Pigeon Pea NADP+ Linked Glucose-6-Phosphate Dehydrogenase. Protein J 36, 49–55 (2017). https://doi.org/10.1007/s10930-017-9702-5

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